ArticleNucleic acids research2007
Recognition of pyrrolysine tRNA by the Desulfitobacterium hafniense pyrrolysyl-tRNA synthetase.
Article in Nucleic acids research, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 57 citations in OpenAlex.
- Genetic Code Expansion: Recent Developments and Emerging Applications.Chemical reviews · 2025Review
- Engineering Pyrrolysine Systems for Genetic Code Expansion and Reprogramming.Chemical reviews · 2024Review
- Evolution of Pyrrolysyl-tRNA Synthetase: From Methanogenesis to Genetic Code Expansion.Chemical reviews · 2024Review
- Engineering tRNAs for the Ribosomal Translation of Non-proteinogenic Monomers.Chemical reviews · 2024Review
- tRNA shape is an identity element for an archaeal pyrrolysyl-tRNA synthetase from the human gut.Nucleic acids research · 2024Article
- The tRNA identity landscape for aminoacylation and beyond.Nucleic acids research · 2023Review
- Update of the Pyrrolysyl-tRNA Synthetase/tRNAJournal of bacteriology · 2023Review
- An efficient cell-free protein synthesis platform for producing proteins with pyrrolysine-based noncanonical amino acids.Biotechnology journal · 2022Article
- Bacterial translation machinery for deliberate mistranslation of the genetic code.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Naturally Occurring tRNAs With Non-canonical Structures.Frontiers in microbiology · 2020Review
- Engineering aminoacyl-tRNA synthetases for use in synthetic biology.The Enzymes · 2020Article
- Linker and N-Terminal Domain Engineering of Pyrrolysyl-tRNA Synthetase for Substrate Range Shifting and Activity Enhancement.Frontiers in bioengineering and biotechnology · 2020Article
- Evolving the N-Terminal Domain of Pyrrolysyl-tRNA Synthetase for Improved Incorporation of Noncanonical Amino Acids.Chembiochem : a European journal of chemical biology · 2018Article
- tRNARNA biology · 2018Review
- The central role of tRNA in genetic code expansion.Biochimica et biophysica acta. General subjects · 2017Review
- Pyrrolysyl-tRNA synthetase, an aminoacyl-tRNA synthetase for genetic code expansion.Croatica chemica acta. Arhiv za kemiju · 2016Article
- tRNA acceptor-stem and anticodon bases embed separate features of amino acid chemistry.RNA biology · 2016Article
- Rationally evolving tRNAPyl for efficient incorporation of noncanonical amino acids.Nucleic acids research · 2015Article
- Ancient horizontal gene transfer and the last common ancestors.BMC evolutionary biology · 2015Article
- Ser or Leu: structural snapshots of mistranslation in Candida albicans.Frontiers in molecular biosciences · 2014Review
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4 authors at 1 institution in 1 country.
Funding
Abstract
Pyrrolysine (Pyl), the 22nd co-translationally inserted amino acid, is incorporated in response to a UAG amber stop codon. Pyrrolysyl-tRNA synthetase (PylRS) attaches Pyl to its cognate tRNA, the special amber suppressor tRNA(Pyl). The genes for tRNA(Pyl) (pylT) and PylRS (pylS) are found in all members of the archaeal family Methanosarcinaceae, and in Desulfitobacterium hafniense. The activation and aminoacylation properties of D. hafniense PylRS and the nature of the tRNA(Pyl) identity elements were determined by measuring the ability of 24 mutant tRNA(Pyl) species to be aminoacylated with the pyrrolysine analog N-epsilon-cyclopentyloxycarbonyl-l-lysine. The discriminator base G73 and the first base pair (G1.C72) in the acceptor stem were found to be major identity elements. Footprinting analysis showed that PylRS binds tRNA(Pyl) predominantly along the phosphate backbone of the T-loop, the D-stem and the acceptor stem. Significant contacts with the anticodon arm were not observed. The tRNA(Pyl) structure contains the highly conserved T-loop contact U54.A58 and position 57 is conserved as a purine, but the canonical T- to D-loop contact between positions 18 and 56 was not present. Unlike most tRNAs, the tRNA(Pyl) anticodon was shown not to be important for recognition by bacterial PylRS.
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